Iron is an essential nutrient for the survival of organisms. Bacterial pathogens possess specialized pathways to acquire heme from their human hosts. In this review, we present recent structural and biochemical data that provide mechanistic insights into several bacterial heme uptake pathways, encompassing the sequestration of heme from human hemoproteins to secreted or membrane-associated bacterial proteins, the transport of heme across bacterial membranes, and the degradation of heme within the bacterial cytosol to liberate iron. The pathways for heme transport into the bacterial cytosol are divergent, harboring non-homologous protein sequences, novel structures, varying numbers of proteins, and different mechanisms. Congruously, the breakdown of heme within the bacterial cytosol by sequence-divergent proteins releases iron and distinct degradation products.
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http://dx.doi.org/10.1016/j.cbpa.2013.12.014 | DOI Listing |
J Proteome Res
January 2025
School of Pharmacy, Department of Pharmaceutical Sciences, University of Maryland, Baltimore, Maryland 21201, United States.
() utilizes heme as an iron source from the host during infection. Biliverdin beta and delta (BVIXβ and BVIXδ) are generated by HemO, specific to , while biliverdin alpha is generated from the bacterial BphO system and by mammalian heme oxygenases. Here, we have developed and characterized a quantitative LC-MS/MS assay for the separation of three endogenous isomers, BVIXα, BVIXβ, and BVIXδ.
View Article and Find Full Text PDFSci Rep
January 2025
Laboratory of Photobiology and Molecular Diagnostics, Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdańsk, Poland.
Staphylococcus aureus (S. aureus) can survive inside nonprofessional phagocytes such as keratinocytes, enabling it to evade antibiotics and cause recurrent infections once treatment stops. New antibacterial strategies to eliminate intracellular, multidrug-resistant bacteria are needed.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Pharmacy and Biotechnology, University of Bologna, Via Irnerio n.42, 40126 Bologna, Italy.
Disaccharide trehalose has been proven in many cases to be particularly effective in preserving the functional and structural integrity of biological macromolecules. In this work, we studied its effect on the electron transfer reactions that occur in the chromatophores of the photosynthetic bacterium . In the presence of a high concentration of trehalose, following the activation of the photochemistry by flashes of light, a slowdown of the electrogenic reactions related to the activity of the photosynthetic reaction center and cytochtome (cyt) complexes is observable.
View Article and Find Full Text PDFBiomolecules
November 2024
Department of Biology, Washington University, St. Louis, MO 63146, USA.
Mitochondrial holocytochrome c synthase (HCCS) is an essential protein in assembling cytochrome c (cyt c) of the electron transport system. HCCS binds heme and covalently attaches the two vinyls of heme to two cysteine thiols of the cyt c CXXCH motif. Human HCCS recognizes both cyt c and cytochrome c of complex III (cytochrome bc).
View Article and Find Full Text PDFAnimals (Basel)
December 2024
Interdisciplinary Center for Aquaculture Research (INCAR), Universidad Andrés Bello, Viña del Mar 2531015, Chile.
is the causative agent of atypical vibriosis in salmonids cultured in Chile. While extensive research provides insights into through phenotypic, antigenic, and genetic typing, as well as various virulence mechanisms, proteomic characterization remains largely unexplored. This study aimed to advance the proteomic knowledge of Chilean Vo-LM-18 and its OMVs, which have known virulence.
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